{"month":"01","title":"Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR","issue":"3","_id":"8471","publication_identifier":{"issn":["0022-2836"]},"doi":"10.1016/j.jmb.2010.11.004","citation":{"short":"H. Van Melckebeke, P. Schanda, J. Gath, C. Wasmer, R. Verel, A. Lange, B.H. Meier, A. Böckmann, Journal of Molecular Biology 405 (2011) 765–772.","apa":"Van Melckebeke, H., Schanda, P., Gath, J., Wasmer, C., Verel, R., Lange, A., … Böckmann, A. (2011). Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2010.11.004\">https://doi.org/10.1016/j.jmb.2010.11.004</a>","ama":"Van Melckebeke H, Schanda P, Gath J, et al. Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. <i>Journal of Molecular Biology</i>. 2011;405(3):765-772. doi:<a href=\"https://doi.org/10.1016/j.jmb.2010.11.004\">10.1016/j.jmb.2010.11.004</a>","ista":"Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A. 2011. Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR. Journal of Molecular Biology. 405(3), 765–772.","chicago":"Van Melckebeke, Hélène, Paul Schanda, Julia Gath, Christian Wasmer, René Verel, Adam Lange, Beat H. Meier, and Anja Böckmann. “Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR.” <i>Journal of Molecular Biology</i>. Elsevier, 2011. <a href=\"https://doi.org/10.1016/j.jmb.2010.11.004\">https://doi.org/10.1016/j.jmb.2010.11.004</a>.","mla":"Van Melckebeke, Hélène, et al. “Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR.” <i>Journal of Molecular Biology</i>, vol. 405, no. 3, Elsevier, 2011, pp. 765–72, doi:<a href=\"https://doi.org/10.1016/j.jmb.2010.11.004\">10.1016/j.jmb.2010.11.004</a>.","ieee":"H. Van Melckebeke <i>et al.</i>, “Probing water accessibility in HET-s(218–289) amyloid fibrils by solid-state NMR,” <i>Journal of Molecular Biology</i>, vol. 405, no. 3. Elsevier, pp. 765–772, 2011."},"type":"journal_article","article_type":"original","oa_version":"None","publisher":"Elsevier","publication_status":"published","volume":405,"extern":"1","author":[{"last_name":"Van Melckebeke","first_name":"Hélène","full_name":"Van Melckebeke, Hélène"},{"first_name":"Paul","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"},{"last_name":"Gath","full_name":"Gath, Julia","first_name":"Julia"},{"full_name":"Wasmer, Christian","first_name":"Christian","last_name":"Wasmer"},{"last_name":"Verel","first_name":"René","full_name":"Verel, René"},{"last_name":"Lange","first_name":"Adam","full_name":"Lange, Adam"},{"last_name":"Meier","first_name":"Beat H.","full_name":"Meier, Beat H."},{"full_name":"Böckmann, Anja","first_name":"Anja","last_name":"Böckmann"}],"language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"765-772","date_created":"2020-09-18T10:11:03Z","abstract":[{"lang":"eng","text":"Despite the importance of protein fibrils in the context of conformational diseases, information on their structure is still sparse. Hydrogen/deuterium exchange measurements of backbone amide protons allow the identification hydrogen-bonding patterns and reveal pertinent information on the amyloid β-sheet architecture. However, they provide only little information on the identity of residues exposed to solvent or buried inside the fibril core. NMR spectroscopy is a potent method for identifying solvent-accessible residues in proteins via observation of polarization transfer between chemically exchanging side-chain protons and water protons. We show here that the combined use of highly deuterated samples and fast magic-angle spinning greatly attenuates unwanted spin diffusion and allows identification of polarization exchange with the solvent in a site-specific manner. We apply this measurement protocol to HET-s(218–289) prion fibrils under different conditions (including physiological pH, where protofibrils assemble together into thicker fibrils) and demonstrate that each protofibril of HET-s(218–289), is surrounded by water, thus excluding the existence of extended dry interfibril contacts. We also show that exchangeable side-chain protons inside the hydrophobic core of HET-s(218–289) do not exchange over time intervals of weeks to months. The experiments proposed in this study can provide insight into the detailed structural features of amyloid fibrils in general."}],"status":"public","intvolume":"       405","publication":"Journal of Molecular Biology","date_updated":"2021-01-12T08:19:30Z","article_processing_charge":"No","quality_controlled":"1","date_published":"2011-01-21T00:00:00Z","year":"2011","day":"21"}